| 1. |
- Marino, Jacopo, et al.
(författare)
-
Small protein domains fold inside the ribosome exit tunnel
- 2016
-
Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 590:5, s. 655-660
-
Tidskriftsartikel (refereegranskat)abstract
- Cotranslational folding of small protein domains within the ribosome exit tunnel may be an important cellular strategy to avoid protein misfolding. However, the pathway of cotranslational folding has so far been described only for a few proteins, and therefore, it is unclear whether folding in the ribosome exit tunnel is a common feature for small protein domains. Here, we have analyzed nine small protein domains and determined at which point during translation their folding generates sufficient force on the nascent chain to release translational arrest by the SecM arrest peptide, both in vitro and in live E. coli cells. We find that all nine protein domains initiate folding while still located well within the ribosome exit tunnel.
|
|
| 2. |
- Nilsson, Ola B., et al.
(författare)
-
Cotranslational Protein Folding inside the Ribosome Exit Tunnel
- 2015
-
Ingår i: Cell Reports. - : Elsevier BV. - 2211-1247. ; 12:10, s. 1533-1540
-
Tidskriftsartikel (refereegranskat)abstract
- At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of co-translational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
|
|
